O16B_CONCL
ID O16B_CONCL Reviewed; 70 AA.
AC D2Y492;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Conotoxin Cal6.11 {ECO:0000305};
DE AltName: Full=Conotoxin Cal6.2 {ECO:0000303|PubMed:21172372};
DE AltName: Full=Conotoxin Cl6.11 {ECO:0000303|PubMed:20363338};
DE AltName: Full=Conotoxin Cl6b {ECO:0000303|PubMed:20363338};
DE Flags: Precursor;
OS Californiconus californicus (California cone) (Conus californicus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Californiconus.
OX NCBI_TaxID=1736779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-70, HYDROXYLATION
RP AT PRO-48 AND PRO-58, GAMMA-CARBOXYGLUTAMATION AT GLU-60 AND GLU-67, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=20363338; DOI=10.1016/j.ympev.2010.03.029;
RA Biggs J.S., Watkins M., Puillandre N., Ownby J.P., Lopez-Vera E.,
RA Christensen S., Moreno K.J., Bernaldez J., Licea-Navarro A., Corneli P.S.,
RA Olivera B.M.;
RT "Evolution of Conus peptide toxins: analysis of Conus californicus Reeve,
RT 1844.";
RL Mol. Phylogenet. Evol. 56:1-12(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=21172372; DOI=10.1016/j.toxicon.2010.12.008;
RA Elliger C.A., Richmond T.A., Lebaric Z.N., Pierce N.T., Sweedler J.V.,
RA Gilly W.F.;
RT "Diversity of conotoxin types from Conus californicus reflects a diversity
RT of prey types and a novel evolutionary history.";
RL Toxicon 57:311-322(2011).
CC -!- FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion
CC channels. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20363338}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:20363338}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; FJ959143; ADB93113.1; -; Genomic_DNA.
DR EMBL; GU306156; ADB04235.1; -; mRNA.
DR AlphaFoldDB; D2Y492; -.
DR ConoServer; 3966; Cal6.11 precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Hydroxylation; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..43
FT /evidence="ECO:0000305|PubMed:20363338"
FT /id="PRO_0000414974"
FT PEPTIDE 45..70
FT /note="Conotoxin Cal6.11"
FT /evidence="ECO:0000269|PubMed:20363338"
FT /id="PRO_0000414975"
FT MOD_RES 48
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:20363338"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:20363338"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000305|PubMed:20363338"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000305|PubMed:20363338"
FT DISULFID 46..57
FT /evidence="ECO:0000250"
FT DISULFID 50..62
FT /evidence="ECO:0000250"
FT DISULFID 56..69
FT /evidence="ECO:0000250"
SQ SEQUENCE 70 AA; 7873 MW; BADA405C6C158880 CRC64;
MKLTCVLIIA VLILTACQFI AADNTEYRKW RRSGTSTGMR LGSRDCGPWC WGQNKCCPDE
SCRSLHESCT
